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Literature summary for 1.14.20.15 extracted from

  • Martinie, R.J.; Livada, J.; Chang, W.C.; Green, M.T.; Krebs, C.; Bollinger, J.M.; Silakov, A.
    Experimental correlation of substrate position with reaction outcome in the aliphatic halogenase, SyrB2 (2015), J. Am. Chem. Soc., 137, 6912-6919.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ dependent on Pseudomonas syringae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Pseudomonas syringae the enzyme catalyzes chlorination of the C4 position of L-threonine appended via a thioester linkage to the phosphopantetheine arm of the companion aminoacyl carrier protein, SyrB1. The native substrate of SyrB2, Thr, is almost exclusively chlorinated, although non-native substrates undergo hydroxylation as well as chlorination. SyrB2 represents an intriguing case in which two different reaction outcomes catalyzed by this enzyme family (hydroxylation and halogenation) are observed ?
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?
additional information Pseudomonas syringae B301D the enzyme catalyzes chlorination of the C4 position of L-threonine appended via a thioester linkage to the phosphopantetheine arm of the companion aminoacyl carrier protein, SyrB1. The native substrate of SyrB2, Thr, is almost exclusively chlorinated, although non-native substrates undergo hydroxylation as well as chlorination. SyrB2 represents an intriguing case in which two different reaction outcomes catalyzed by this enzyme family (hydroxylation and halogenation) are observed ?
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?

Organism

Organism UniProt Comment Textmining
Pseudomonas syringae
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Pseudomonas syringae B301D
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme catalyzes chlorination of the C4 position of L-threonine appended via a thioester linkage to the phosphopantetheine arm of the companion aminoacyl carrier protein, SyrB1. The native substrate of SyrB2, Thr, is almost exclusively chlorinated, although non-native substrates undergo hydroxylation as well as chlorination. SyrB2 represents an intriguing case in which two different reaction outcomes catalyzed by this enzyme family (hydroxylation and halogenation) are observed Pseudomonas syringae ?
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?
additional information non-native substrates undergo hydroxylation as well as chlorination. The cis-chloroferryl complex in enzyme SyrB2 reacts more rapidly with SyrB1 presenting L-aminobutyric acid or L-norvaline than with L-threonine. Selectivity for chlorination is also strongly modulated: L-threonine is almost exclusively chlorinated, L-aminobutyric acid is chlorinated and hydroxylated at C4 to similar extents, and L-norvaline is predominately hydroxylated at the C5 position. The differential reactivity observed for the different substrates might arise primarily from substrate-protein interactions that impact the partition between the axial and equatorial coordination isomers of the ferryl complex rather than from substrate positioning per se Pseudomonas syringae ?
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?
additional information the enzyme catalyzes chlorination of the C4 position of L-threonine appended via a thioester linkage to the phosphopantetheine arm of the companion aminoacyl carrier protein, SyrB1. The native substrate of SyrB2, Thr, is almost exclusively chlorinated, although non-native substrates undergo hydroxylation as well as chlorination. SyrB2 represents an intriguing case in which two different reaction outcomes catalyzed by this enzyme family (hydroxylation and halogenation) are observed Pseudomonas syringae B301D ?
-
?
additional information non-native substrates undergo hydroxylation as well as chlorination. The cis-chloroferryl complex in enzyme SyrB2 reacts more rapidly with SyrB1 presenting L-aminobutyric acid or L-norvaline than with L-threonine. Selectivity for chlorination is also strongly modulated: L-threonine is almost exclusively chlorinated, L-aminobutyric acid is chlorinated and hydroxylated at C4 to similar extents, and L-norvaline is predominately hydroxylated at the C5 position. The differential reactivity observed for the different substrates might arise primarily from substrate-protein interactions that impact the partition between the axial and equatorial coordination isomers of the ferryl complex rather than from substrate positioning per se Pseudomonas syringae B301D ?
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?

Synonyms

Synonyms Comment Organism
aliphatic halogenase
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Pseudomonas syringae
SyrB2
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Pseudomonas syringae

General Information

General Information Comment Organism
evolution the enzyme SyrB2 from Pseudomonas syringae B301D is the founding member of the Fe/2OG aliphatic halogenases. In SyrB2, the sequence position that normally provides the carboxylate of the canonical facial triad of protein ligands is occupied by an alanine (Ala118), and the co-substrate, chloride (Cl?), occupies the vacated site in the iron coordination sphere.32 Fe/2OG halogenases mechanistically parallel the hydroxylases in that both employ ferryl intermediates as the H•-abstracting species Pseudomonas syringae
additional information other factors might be involved in directing the halogenation outcome and the likelihood that proper substrate positioning is also essential to avoidance of hydroxylation in the other types of Fe/2OG-oxygenase reactivity, direct probing the positions of the various target C-H bonds relative to the iron center, coupling of NO, overview Pseudomonas syringae